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B6db references: 28097768

type Journal Article
authors Kawata J, Naoe T, Ogasawara Y, Dairi T
title Biosynthesis of the Carbonylmethylene Structure Found in the Ketomemicin Class of Pseudotripeptides
journal Angew Chem Int Ed Engl
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ui 28097768
year (2017)
volume 56
number 8
pages 2026-2029
keywords biosynthesis; enzymes; natural products; peptidomimetics; pseudopeptides
abstract We recently discovered novel pseudotripeptides, the ketomemicins, which possess a C-terminal pseudodipeptide connected with a carbonylmethylene instead of an amide bond, through heterologous expression of gene clusters identified in actinobacteria. The carbonylmethylene structure is a stable isostere of the amide bond and its biological significance has been shown in several natural and synthetic products. Despite the biological importance of these compounds, little is known about how the carbonylmethylene structure is biosynthesized. In this work, we fully characterized the biosynthetic machinery of the pseudodipeptide. An aldolase, dehydratase, PLP-dependent glycine-C-acetyltransferase, and dehydrogenase were involved in the formation of the pseudodipeptide, with malonyl-CoA and phenylpyruvate as starter substrates.
last changed 2018/02/26 09:40

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